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Literature summary for 1.14.14.18 extracted from

  • Davydov, R.; Kofman, V.; Fujii, H.; Yoshida, T.; Ikeda-Saito, M.; Hoffman, B.M.
    Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants (2002), J. Am. Chem. Soc., 124, 1798-1808.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of truncated heme oxygenase-1 in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D140A mutant of truncated heme oxygenase-1 Rattus norvegicus
D140F mutant of truncated heme oxygenase-1 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O hydroperoxoferri-heme oxygenase-1 is the reactive species directly forming the alpha-meso-hydroxyheme product by attack of the distal OH of the hydroperoxo moiety at the heme alpha-carbon Rattus norvegicus